Open AccessSpecificity of a heme‐assimilating system of Vibrio vulnificus to synthetic heme compounds
Author(s) -
Miyoshi Shinichi,
Kamei Takehito,
Ota Yoko,
Masunaga Chiaki,
Izuhara Yuko,
Tomochika Kenichi,
Shinoda Sumio,
Yamamoto Shigeo
Publication year - 2002
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2002.tb11063.x
Subject(s) - vibrio vulnificus , porphyrin , heme , chemistry , strain (injury) , bacteria , stereochemistry , biochemistry , biology , enzyme , genetics , anatomy
Vibrio vulnificus strain L‐180, a clinical isolate, can obtain iron from a synthetic heme, iron–tetra(4‐sulfonatophenyl)porphyrin (Fe–TPPS), as well as from a natural heme, protoheme. This assimilation of iron bound to TPPS was demonstrated to be a common property of V. vulnificus by testing a total of 27 strains isolated from both clinical and environmental sources. Strain L‐180 could also utilize Fe–TCPP, but not Fe–TMPyP, as a sole iron source. TPPS or its complex with a metal ion reduced bacterial multiplication in the broth containing a minimum dose of Fe–TPPS. When inoculated into human serum supplemented with Fe–TCPP, L‐180 could grow only in the presence of a protease from the same bacterium. In both TPPS and TCPP, each side chain of a porphyrin ring has a negative charge. Therefore, this negative charge may be important for interaction with an outer membrane receptor involving in a heme‐assimilating system of V. vulnificus .